Search

Your search keyword '"Mason, James M."' showing total 8 results
Start Over Author "Mason, James M." Journal plos one
8 results on '"Mason, James M."'

6. Utility of Biomarkers in the Differential Diagnosis of Heart Failure in Older People: Findings from the Heart Failure in Care Homes (HFinCH) Diagnostic Accuracy Study

Author

Mason, James M., primary, Hancock, Helen C., additional, Close, Helen, additional, Murphy, Jerry J., additional, Fuat, Ahmet, additional, de Belder, Mark, additional, Singh, Raj, additional, Teggert, Andrew, additional, Wood, Esther, additional, Brennan, Gill, additional, Hussain, Nehal, additional, Kumar, Nitin, additional, Manshani, Novin, additional, Hodges, David, additional, Wilson, Douglas, additional, and Hungin, A. Pali S., additional

Published
2013
Full Text
View/download PDF

8. Phosphorylation at Serines 216 and 221 Is Important for Drosophila HeT-A Gag Protein Stability.

Author

Brar, Sukhdev S., Petrovich, Robert M., Williams, Jason G., and Mason, James M.

Subjects
PHOSPHORYLATION, SERINE, DROSOPHILA, GAG proteins, PROTEIN stability, TELOMERASE, CHROMOSOMAL translocation
Abstract

Telomeres from Drosophila appear to be very different from those of other organisms – in size and the mechanism of their maintenance. In the absence of the enzyme telomerase, Drosophila telomeres are maintained by retrotransposition of three elements, HeT-A, TART, and TAHRE, but details of their transposition mechanisms are not known. Here we characterized some biochemical characteristics of the HeT-A Gag protein encoded by the HeT-A element to understand this mechanism. The HeT-A Gag protein when overexpressed in S2 cells was localized to the nucleus but was resistant to high salt, detergents and nuclease extraction treatments. Analysis of the HeT-A Gag protein by tandem mass spectrophotometry revealed that serines 216 and 221 are phosphorylated. Substituting these serines with alanine or aspartic acid by site-directed mutagenesis did not result in any changes in HeT-A Gag translocation across the nucleus, suggesting that phosphorylation of these sites is not associated with HeT-A Gag translocation, but time course experiments showed that these phosphorylation sites are important for Gag-protein stability. [ABSTRACT FROM AUTHOR]

Published
2013
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results